WordNet

be a contributing factor; "make things factor into a companys profitability"
any of the numbers (or symbols) that form a product when multiplied together
an independent variable in statistics
anything that contributes causally to a result; "a number of factors determined the outcome"
consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
a concept whose truth can be proved; "scientific hypotheses are not facts"
a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"
the 9th letter of the Roman alphabet (同)i

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(…の)『要因』,(…を生み出す)要素《+『in』+『名』(do『ing』)》 / 囲数,約数 / 代理人,《おもに英》仲買人 / =factorize
〈C〉『事実』,実際にある(あった)事 / 〈U〉真相,真実(truth) / 《the~》(法律用語で)犯行
『私は』私が
iodineの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/27 19:40:44」(JST)

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Role of thrombin in the blood coagulation cascade

Thrombin (EC 3.4.21.5, fibrinogenase, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation factor II, blood-coagulation factor IIa, factor IIa, E thrombin, beta-thrombin, gamma-thrombin) is a serine protease that in humans is encoded by the F2 gene.^[2]^[3] Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions.

History

After the description of fibrinogen and fibrin, Alexander Schmidt hypothesised the existence of an enzyme that converts fibrinogen into fibrin in 1872.^[4]

Physiology

Synthesis

Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). The activity of factor Xa is greatly enhanced by binding to activated Factor V (Va), termed the prothrombinase complex. Prothrombin is produced in the liver and is post-translationally modified in a vitamin K-dependent reaction that converts ten glutamic acids on prothrombin to gamma-carboxyglutamic acid (Gla). In the presence of calcium, the Gla residues promote the binding of prothrombin to phospholipid bilayers. Deficiency of vitamin K or administration of the anticoagulant warfarin inhibits the production of gamma-carboxyglutamic acid residues, slowing the activation of the coagulation cascade.

In human adults, the normal blood level of antithrombin activity has been measured to be around 1.1 units/mL. Newborn levels of thrombin steadily increase after birth to reach normal adult levels, from a level of around 0.5 units/mL 1 day after birth, to a level of around 0.9 units/mL after 6 months of life.^[5]

Mechanism of action

In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa.

Factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between lysine and glutamine residues in fibrin. The covalent bonds increase the stability of the fibrin clot. Thrombin interacts with thrombomodulin.^[6]^[7]

As part of its activity in the coagulation cascade, thrombin also promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet.

Negative feedback

Thrombin bound to thrombomodulin activates protein C, an inhibitor of the coagulation cascade. The activation of protein C is greatly enhanced following the binding of thrombin to thrombomodulin, an integral membrane protein expressed by endothelial cells. Activated protein C inactivates factors Va and VIIIa. Binding of activated protein C to protein S leads to a modest increase in its activity. Thrombin is also inactivated by antithrombin, a serine protease inhibitor.

Protein

Anchoring of bovine prothrombin to the membrane through its Gla domain.^[8]

The molecular weight of prothrombin is approximately 72,000 Da. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36,000 Da. Structurally, it is a member of the large PA clan of proteases.

Gene

The thrombin (prothrombin) gene is located on the eleventh chromosome (11p11-q12).^[2]

There are an estimated 30 people in the world that have been diagnosed with the congenital form of Factor II deficiency,^[9] which should not be confused with the prothrombin G20210A mutation, which is also called the factor II mutation. Prothrombin G20210A is congenital.^[10]

Prothrombin G20210A is not usually accompanied by other factor mutations (i.e., the most common is factor V Leiden). The gene may be inherited heterozygous (1 pair), or much more rarely, homozygous (2 pairs), and is not related to gender or blood type. Homozygous mutations increase the risk of thrombosis more than heterozygous mutations, but the relative increased risk is not well documented. Other potential risks for thrombosis, such as oral contraceptives may be additive. The previously reported relationship of inflammatory bowel disease (i.e., Crohn's disease or ulcerative colitis) and prothrombin G20210A or factor V Leiden mutation have been contradicted by research.^[11]

Role in disease

Activation of prothrombin is crucial in physiological and pathological coagulation. Various rare diseases involving prothrombin have been described (e.g., hypoprothrombinemia). Anti-prothrombin antibodies in autoimmune disease may be a factor in the formation of the lupus anticoagulant also known as (antiphospholipid syndrome). Hyperprothrombinemia can be caused by the G20210A mutation.

Thrombin, a potent vasoconstrictor and mitogen, is implicated as a major factor in vasospasm following subarachnoid hemorrhage. Blood from a ruptured cerebral aneurysm clots around a cerebral artery, releasing thrombin. This can induce an acute and prolonged narrowing of the blood vessel, potentially resulting in cerebral ischemia and infarction (stroke).

Beyond its key role in the dynamic process of thrombus formation, thrombin has a pronounced pro-inflammatory character, which may influence the onset and progression of atherosclerosis. Acting via its specific cell membrane receptors (protease activated receptors: PAR-1, PAR-3 and PAR-4), which are abundantly expressed in all arterial vessel wall constituents, thrombin has the potential to exert pro-atherogenic actions such as inflammation, leukocyte recruitment into the atherosclerotic plaque, enhanced oxidative stress, migration and proliferation of vascular smooth muscle cells, apoptosis and angiogenesis.^[12]^[13]^[14]

Thrombin is implicated in the physiology of blood clots. Its presence indicates the existence of a clot. In 2013 a system for detecting the presence of thrombin was developed in mice. It combines peptide-coated iron oxide attached to "reporter chemicals". When a peptide binds to a thrombin molecule, the report is released and appears in the urine where it can be detected. Human testing has not been conducted.^[15]

Applications

Research tool

Due to its high proteolytic specificity, thrombin is a valuable biochemical tool. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is commonly included in linker regions of recombinant fusion protein constructs. Following purification of the fusion protein, thrombin can be used to selectively cleave between the Arginine and Glycine residues of the cleavage site, effectively removing the purification tag from the protein of interest with a high degree of specificity.

Medicine and surgery

Prothrombin complex concentrate and fresh frozen plasma are prothrombin-rich coagulation factor preparations that can be used to correct deficiencies (usually due to medication) of prothrombin. Indications include intractable bleeding due to warfarin.

Manipulation of prothrombin is central to the mode of action of most anticoagulants. Warfarin and related drugs inhibit vitamin K-dependent carboxylation of several coagulation factors, including prothrombin. Heparin increases the affinity of antithrombin to thrombin (as well as factor Xa). The direct thrombin inhibitors, a newer class of medication, directly inhibit thrombin by binding to its active site.

Recombinant thrombin is available as a powder for reconstitution into aqueous solution. It can be applied topically during surgery, as an aid to hemostasis. It can be useful for controlling minor bleeding from capillaries and small venules, but ineffective and not indicated for massive or brisk arterial bleeding.^[16]^[17]^[18]

Food production

Thrombin is sold under the brand name Fibrimex for use as a binding agent for meat. The thrombin in Fibrimex derives from porcine or bovine blood.^[19] According to the manufacturer it can be used to produce new kinds of mixed meats (for example combining beef and fish seamlessly). The manufacturer also states that it can be used to combine whole muscle meat, form and portion these thus cutting down on production costs without a loss in quality.^[20]

General secretary Jan Bertoft of Swedish Consumers' Association has stated that "there is danger of misleading the consumers since there is no way to tell this reconstituted meat from real meat"^[19]

References

^ PDB 2C93; Howard N, Abell C, Blakemore W, Chessari G, Congreve M, Howard S, Jhoti H, Murray CW, Seavers LC, van Montfort RL (February 2006). "Application of fragment screening and fragment linking to the discovery of novel thrombin inhibitors". J. Med. Chem. 49 (4): 1346–55. doi:10.1021/jm050850v. PMID 16480269.
^ ^a ^b Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somat. Cell Mol. Genet. 13 (3): 285–92. doi:10.1007/BF01535211. PMID 3474786.
^ Degen SJ, Davie EW (September 1987). "Nucleotide sequence of the gene for human prothrombin". Biochemistry 26 (19): 6165–77. doi:10.1021/bi00393a033. PMID 2825773.
^ Schmidt A (1872). "Neue Untersuchungen ueber die Fasserstoffesgerinnung". Pflüger's Archiv für die gesamte Physiologie 6: 413–538. doi:10.1007/BF01612263.
^ Andrew M, Paes B et al. (1987). "Development of the human coagulation system in the full-term infant". Blood 70 (1): 165–172. PMID 3593964.
^ Bajzar L, Morser J, Nesheim M (July 1996). "TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex". J. Biol. Chem. 271 (28): 16603–8. doi:10.1074/jbc.271.28.16603. PMID 8663147.
^ Jakubowski HV, Owen WG (July 1989). "Macromolecular specificity determinants on thrombin for fibrinogen and thrombomodulin". J. Biol. Chem. 264 (19): 11117–21. PMID 2544585.
^ PDB 1nl2; Huang M, Rigby AC, Morelli X, Grant MA, Huang G, Furie B, Seaton B, Furie BC (September 2003). "Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins". Nat. Struct. Biol. 10 (9): 751–6. doi:10.1038/nsb971. PMID 12923575.
^ Degen SJ, McDowell SA, Sparks LM, Scharrer I (February 1995). "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala". Thromb. Haemost. 73 (2): 203–9. PMID 7792730.
^ Varga EA, Moll S (July 2004). "Cardiology patient pages. Prothrombin 20210 mutation (factor II mutation)". Circulation 110 (3): e15–8. doi:10.1161/01.CIR.0000135582.53444.87. PMID 15262854.
^ Bernstein CN, Sargent M et al. (2007). "Mutations in clotting factors and inflammatory bowel disease". Am. J. Gastroenterol. 102 (2): 338–343. doi:10.1111/j.1572-0241.2006.00974.x. PMID 17156138.
^ Borissoff JI, Spronk HM, Heeneman S, ten Cate H (June 2009). "Is thrombin a key player in the 'coagulation-atherogenesis' maze?". Cardiovasc. Res. 82 (3): 392–403. doi:10.1093/cvr/cvp066. PMID 19228706.
^ Borissoff JI, Heeneman S, Kilinç E, Kassák P, Van Oerle R, Winckers K, Govers-Riemslag JW, Hamulyák K, Hackeng TM, Daemen MJ, ten Cate H, Spronk HM (August 2010). "Early atherosclerosis exhibits an enhanced procoagulant state". Circulation 122 (8): 821–30. doi:10.1161/CIRCULATIONAHA.109.907121. PMID 20697022.
^ Borissoff JI, Spronk HM, ten Cate H (May 2011). "The hemostatic system as a modulator of atherosclerosis". N. Engl. J. Med. 364 (18): 1746–60. doi:10.1056/NEJMra1011670. PMID 21542745.
^ Economist (2013-11-05). "Nanomedicine: Particle physiology". The Economist. Retrieved 2013-12-15.
^ Chapman WC, Singla N, Genyk Y, McNeil JW, Renkens KL, Reynolds TC, Murphy A, Weaver FA (August 2007). "A phase 3, randomized, double-blind comparative study of the efficacy and safety of topical recombinant human thrombin and bovine thrombin in surgical hemostasis". J. Am. Coll. Surg. 205 (2): 256–65. doi:10.1016/j.jamcollsurg.2007.03.020. PMID 17660072.
^ Singla NK, Ballard JL, Moneta G, Randleman CD, Renkens KL, Alexander WA (July 2009). "A phase 3b, open-label, single-group immunogenicity and safety study of topical recombinant thrombin in surgical hemostasis". J. Am. Coll. Surg. 209 (1): 68–74. doi:10.1016/j.jamcollsurg.2009.03.016. PMID 19651065.
^ Greenhalgh DG, Gamelli RL, Collins J, Sood R, Mozingo DW, Gray TE, Alexander WA (2009). "Recombinant thrombin: safety and immunogenicity in burn wound excision and grafting". J Burn Care Res 30 (3): 371–9. doi:10.1097/BCR.0b013e3181a28979. PMID 19349898.
^ ^a ^b "Sverige röstade ja till köttklister" [Sweden voted in favor of the meat paste] (in Swedish). Dagens Nyheter. 2010-02-09. Retrieved 2010-10-17.
^ "Welcome to Fibrimex". Fibrimex website. FX Technology. Retrieved 2010-10-17.

External links

The MEROPS online database for peptidases and their inhibitors: S01.217
GeneReviews/NCBI/NIH/UW entry on Prothrombin Thrombophilia
Anti-coagulation & proteases on YouTube by The Proteolysis Map-animation
[3] PMAP: The Proteolysis Map/Thrombin
Thrombin: RCSB PDB Molecule of the Month

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. プロトロンビン遺伝子突然変異：血栓症リスクおよび診断 prothrombin gene mutation thrombotic risk and diagnosis
2. 止血の概要 overview of hemostasis
3. 抗リン脂質抗体症候群の治療 treatment of the antiphospholipid syndrome
4. 傍神経節腫および褐色細胞腫：悪性疾患のマネージメント paraganglioma and pheochromocytoma management of malignant disease
5. 非膵島細胞腫瘍性低血糖 nonislet cell tumor hypoglycemia

English Journal

Separation and preconcentration of Cu(II), Pb(II), Zn(II), Fe(III) and Cr(III) ions with coprecipitation method without carrier element and their determination in food and water samples.

Mendil D1, Karatas M2, Tuzen M2.
Food chemistry.Food Chem.2015 Jun 15;177:320-4. doi: 10.1016/j.foodchem.2015.01.008. Epub 2015 Jan 12.
In this study, Cu(II), Pb(II), Zn(II), Fe(III) and Cr(III) were determined in some food and water samples after development 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline (BCP) coprecipitation procedure using flame atomic absorption spectrometry (FAAS). Effects of some analytical parameter including
PMID 25660892

Mercury (II) sensor based on monitoring dissociation rate of the trans-acting factor MerR from cis-element by surface plasmon resonance.

Taniguchi M1, Siddiki MS1, Ueda S1, Maeda I2.
Biosensors & bioelectronics.Biosens Bioelectron.2015 May 15;67:309-14. doi: 10.1016/j.bios.2014.08.040. Epub 2014 Aug 23.
Transcriptional switches regulate gene expression in response to environmental changes surrounding cell. Many studies have focused on two fundamentally different models of transcriptional control by bacterial metalloregulatory protein. Distortion of the DNA fragment including cis-element, to which t
PMID 25190091

Epidermal growth factor receptor inhibitor protects against abdominal aortic aneurysm in a mouse model.

Obama T1, Tsuji T1, Kobayashi T1, Fukuda Y1, Takayanagi T1, Taro Y1, Kawai T1, Forrester SJ1, Elliott KJ1, Choi E2, Daugherty A3, Rizzo V1, Eguchi S1.
Clinical science (London, England : 1979).Clin Sci (Lond).2015 May 1;128(9):559-65. doi: 10.1042/CS20140696.
Angiotensin II (Ang II) has been implicated in the development of abdominal aortic aneurysm (AAA). In vascular smooth muscle cells (VSMC), Ang II activates epidermal growth factor receptor (EGFR) mediating growth promotion. We hypothesized that inhibition of EGFR prevents Ang II-dependent AAA. C57BL
PMID 25531554

Japanese Journal

Involvement of autophagy in the pharmacological effects of the mTOR inhibitor everolimus in acute kidney injury.

Nakagawa Shunsaku,Nishihara Kumiko,Inui Ken-Ichi,Masuda Satohiro
European journal of pharmacology 696(1-3), 143-154, 2012-12-05
… Using cells from normal kidney epithelial cell lines, we found that the antiproliferative effects of mTOR inhibitor everolimus accompanied the accumulation of a marker for cellular autophagic activity, the phosphatidylethanolamine-conjugated form of microtubule-associated protein 1 light chain 3 (LC3-II) in cells. … We also showed that the primary autophagy factor UNC-51-like kinase 1 was involved in the antiproliferative effects of everolimus. …
NAID 120004996384

Endothelial PI3K-C2α, a class II PI3K, has an essential role in angiogenesis and vascular barrier function

Yoshioka Kazuaki,Yoshida Kotaro,Cui Hong,Wakayama Tomohiko,Takuwa Noriko,Okamoto Yasuo,Du Wa,Qi Xun,Asanuma Ken,Sugihara Kazushi,Aki Sho,Miyazawa Hidekazu,Biswas Kuntal,Nagakura Chisa,Ueno Masaya,Iseki Shoichi,Schwartz Robert J.,Okamoto Hiroshi,Sasaki Takehiko,Matsui Osamu,Asano Masahide,Adams Ralf H.,Takakura Nobuyuki,Takuwa Yoh
Nature Medicine 18(10), 1560-1569, 2012-10
… The class II α-isoform of phosphatidylinositol 3-kinase (PI3K-C2α) is localized in endosomes, the trans-Golgi network and clathrin-coated vesicles; … PI3K-C2α knockdown also impaired endothelial cell signaling, including vascular endothelial growth factor receptor internalization and endosomal RhoA activation. …
NAID 120004966617

遊びにおける幼児の身振りの様相とその意味 : 3歳児の関係性と身振りに着目して(第1部自由論文)

海野摩也子,藤田清澄
保育学研究 50(1), 6-19, 2012-08-31
… 次に【研究II】では,【研究I】で多く身振りがみられた女児の集団を追いかけて観察し,質的に分析を行った。 …
NAID 110009490128

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★リンクテーブル★

リンク元	「プロトロンビン」
拡張検索	「insulin-like growth factor II」「heparin cofactor II」「factor III」
関連記事	「II」「I」「fact」「factor」

「プロトロンビン」

Coagulation factor II (thrombin)
	; The structure of human thrombin in complex with the inhibitor hirudin.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1A2C, 1A3B, 1A3E, 1A46, 1A4W, 1A5G, 1A61, 1ABI, 1ABJ, 1AD8, 1AE8, 1AFE, 1AHT, 1AI8, 1AIX, 1AWF, 1AWH, 1AY6, 1B5G, 1B7X, 1BA8, 1BB0, 1BCU, 1BHX, 1BMM, 1BMN, 1BTH, 1C1U, 1C1V, 1C1W, 1C4U, 1C4V, 1C4Y, 1C5L, 1C5N, 1C5O, 1CA8, 1D3D, 1D3P, 1D3Q, 1D3T, 1D4P, 1D6W, 1D9I, 1DE7, 1DIT, 1DM4, 1DOJ, 1DWB, 1DWC, 1DWD, 1DWE, 1DX5, 1E0F, 1EB1, 1EOJ, 1EOL, 1FPC, 1FPH, 1G30, 1G32, 1G37, 1GHV, 1GHW, 1GHX, 1GHY, 1GJ4, 1GJ5, 1H8D, 1H8I, 1HAG, 1HAH, 1HAI, 1HAO, 1HAP, 1HBT, 1HDT, 1HGT, 1HLT, 1HUT, 1HXE, 1HXF, 1IHS, 1IHT, 1JMO, 1JOU, 1JWT, 1K21, 1K22, 1KTS, 1KTT, 1LHC, 1LHD, 1LHE, 1LHF, 1LHG, 1MH0, 1MU6, 1MU8, 1MUE, 1NM6, 1NO9, 1NRN, 1NRO, 1NRP, 1NRQ, 1NRR, 1NRS, 1NT1, 1NU7, 1NU9, 1NY2, 1NZQ, 1O0D, 1O2G, 1O5G, 1OOK, 1OYT, 1P8V, 1PPB, 1QBV, 1QHR, 1QJ1, 1QJ6, 1QJ7, 1QUR, 1RD3, 1RIW, 1SB1, 1SFQ, 1SG8, 1SGI, 1SHH, 1SL3, 1SR5, 1T4U, 1T4V, 1TA2, 1TA6, 1TB6, 1TBZ, 1THP, 1THR, 1THS, 1TMB, 1TMT, 1TMU, 1TOM, 1TQ0, 1TQ7, 1TWX, 1UMA, 1UVS, 1VR1, 1VZQ, 1W7G, 1WAY, 1WBG, 1XM1, 1XMN, 1YPE, 1YPG, 1YPJ, 1YPK, 1YPL, 1YPM, 1Z71, 1Z8I, 1Z8J, 1ZGI, 1ZGV, 1ZRB, 2A0Q, 2A2X, 2A45, 2AFQ, 2ANK, 2ANM, 2B5T, 2BDY, 2BVR, 2BVS, 2BVX, 2BXT, 2BXU, 2C8W, 2C8X, 2C8Y, 2C8Z, 2C90, 2C93, 2CF8, 2CF9, 2CN0, 2FEQ, 2FES, 2GDE, 2GP9, 2H9T, 2HGT, 2HNT, 2HPP, 2HPQ, 2HWL, 2JH0, 2JH5, 2JH6, 2OD3, 2PGB, 2PGQ, 2PKS, 2PW8, 2R2M, 2THF, 2UUF, 2UUJ, 2UUK, 2V3H, 2V3O, 2ZC9, 2ZDA, 2ZDV, 2ZF0, 2ZFF, 2ZFP, 2ZFQ, 2ZFR, 2ZG0, 2ZGB, 2ZGX, 2ZHE, 2ZHF, 2ZHQ, 2ZHW, 2ZI2, 2ZIQ, 2ZNK, 2ZO3, 3B23, 3B9F, 3BEF, 3BEI, 3BF6, 3BIU, 3BIV, 3BV9, 3C1K, 3C27, 3D49, 3DA9, 3DD2, 3DHK, 3DT0, 3DUX, 3E6P, 3EE0, 3EGK, 3EQ0, 3F68, 3GIC, 3GIS, 3HAT, 3HKJ, 3HTC, 3JZ1, 3JZ2, 3K65, 3LDX, 3LU9, 3NXP, 3P17, 3P6Z, 3P70, 3PMH, 3PO1, 3QDZ, 3QGN, 3QLP, 3QTO, 3QTV, 3QWC, 3QX5, 3R3G, 3RLW, 3RLY, 3RM0, 3RM2, 3RML, 3RMM, 3RMN, 3RMO, 3S7H, 3S7K, 3SHA, 3SHC, 3SI3, 3SI4, 3SQE, 3SQH, 3SV2, 3T5F, 3TU7, 3U69, 3U8O, 3U8R, 3U8T, 3U98, 3U9A, 3UTU, 3UWJ, 3VXE, 3VXF, 4AX9, 4AYV, 4AYY, 4AZ2, 4BAH, 4BAK, 4BAM, 4BAN, 4BAO, 4BAQ, 4BOH, 4CH2, 4CH8, 4DIH, 4DII, 4DT7, 4DY7, 4E05, 4E06, 4E7R, 4H6S, 4H6T, 4HFP, 4HFY, 4HTC, 4HZH, 4I7Y, 4LZ1, 4LZ4, 4MLF, 4N3L, 4NZE, 4NZQ, 4O03, 4THN, 5GDS, 7KME, 8KME
Identifiers
Symbols	F2 ; PT; RPRGL2; THPH1
External IDs	OMIM: 176930 MGI: 88380 HomoloGene: 426 IUPHAR: 2362 ChEMBL: 204 GeneCards: F2 Gene
EC number	3.4.21.5
Gene ontology
Molecular function	• serine-type endopeptidase activity; • receptor binding; • calcium ion binding; • protein binding; • growth factor activity; • thrombospondin receptor activity;
Cellular component	• extracellular region; • extracellular space; • endoplasmic reticulum lumen; • Golgi lumen; • plasma membrane; • extracellular vesicular exosome; • blood microparticle;
Biological process	• positive regulation of protein phosphorylation; • proteolysis; • acute-phase response; • cell surface receptor signaling pathway; • multicellular organismal development; • blood coagulation; • blood coagulation, intrinsic pathway; • positive regulation of cell proliferation; • regulation of cell shape; • response to wounding; • negative regulation of platelet activation; • positive regulation of phosphatidylinositol 3-kinase signaling; • peptidyl-glutamic acid carboxylation; • platelet activation; • regulation of blood coagulation; • positive regulation of blood coagulation; • positive regulation of cell growth; • positive regulation of collagen biosynthetic process; • fibrinolysis; • post-translational protein modification; • cellular protein metabolic process; • negative regulation of proteolysis; • negative regulation of astrocyte differentiation; • leukocyte migration; • positive regulation of release of sequestered calcium ion into cytosol; • cytosolic calcium ion homeostasis; • negative regulation of fibrinolysis; • positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway; • positive regulation of reactive oxygen species metabolic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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